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β6-N-Acetylglucosaminyltransferase (IGnT)

  • Minoru Fukuda

Abstract

I-branching β6-N-acetylglucosaminyltransferase (IGnT) is a glycosyltransferase that catalyzes the transfer of GlcNAc from UDP-GlcNAc to β1,4-linked Gal residue in a linear poly-N-acetyllactosamine, ±Galβ1-4GlcNAcβ1-3Galβ1-4Glc(NAc)-R, forming ±Galβ1-4GlcNAcβ1-3(GlcNAcβ1-6)Galβ1-4Glc(NAc)-R. The formation of the I branch is usually followed by galactosylation with β4-galactosyltransferase I, resulting in the I antigen. The I-antigen can be further modified to express functional oligosaccharides, such as sialyl Lewis X (Fig. 1).
Fig. 1

Biosynthetic steps of I-branches containing sialyl Lewis X termini. A linear poly-N-acetyllactosamine (i-antigen) is converted to a branched poly-N-acetyllactosamine (I-antigen) by the actions of cIGnT and β4-galactosyltransferase. By dIGnT, a branch is added to GlcNAcB1-3Galβ1-4GlcN(Ac)βl-R acceptor. I-branched poly-N-acetyllactosamines can be further modified to express sialyl Lewis X by the actions of α3-sialyltransferase and α3-fucosyltransferase (Fuc-TVII)

Keywords

Embryonal Carcinoma Cell Galactose Residue Bovine Colostrum Human Teratocarcinoma Cell Functional Oligosaccharide 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Japan 2002

Authors and Affiliations

  • Minoru Fukuda
    • 1
  1. 1.Glycobiology ProgramThe Burnham InstituteLa JollaUSA

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